Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (hereinafter, referred to as MALT1) is cysteine protease, and activates the signal transduction of nuclear factor kappa-light-chain-enhancer of activated B cells (hereinafter, referred to as NF-κB) by decomposing proteins such as A20 and CYLD, responsible for the negative feedback mechanism of the transcriptional activity of the NF-κB (Beyaert et al., Nature Immunology, 2008, Vol. 9, p. 263-271 and Beyaert et al., The EMBO Journal, 2011, Vol. 30, p. 1742-1752).
NF-κB signals control immune responses such as the survival, differentiation, and activation of B cells and T cells. It is known that excessive activation of NF-κB signals by the increased protease activity of MALT1 may cause various types of autoimmune disease. For example, in MALT lymphoma or activated B-cell-like diffuse large B-cell lymphoma (ABC-DLBCL), the protease activity of MALT1 is increased and involved in the occurrence of diseases involving immunological abnormality (Staudt et al., Nature, 2006, Vol. 441, p. 106-110).
It has been reported as to experimental autoimmune encephalomyelitis models, which are typical animal models of multiple sclerosis, that deficiency in MALT1 gene (mucosa-associated lymphoid tissue lymphoma translocation gene 1; hereinafter, referred to as MALT1 gene) completely suppresses the pathological condition thereof. Therefore, it has also been reported that the inhibition of the protease activity of MALT1 is effective for the treatment or prevention of multiple sclerosis (Mak et al., The Journal of Clinical Investigation, 2012, Vol. 122, p. 4698-4709).
The association of autoimmune disease with proteins such as A20 and CYLD, which are decomposed and deactivated by MALT1 has also been reported. For example, it has been reported that autoimmune disease-like pathological conditions such as rheumatism, psoriasis, and colitis occur spontaneously in mice deficient in a gene encoding A20 (Ma et al., Science, 2000, Vol. 289, p. 2350-2354).
It has been reported as to dinitrofluorobenzene-induced dermatitis models, which are typical animal models of contact dermatitis, that deficiency in MALT1 gene remarkably suppresses the pathological condition thereof; thus the inhibition of the protease activity of MALT1 can be expected to produce therapeutic and prophylactic effects on contact dermatitis (Klemm et al., The Journal of Experimental Medicine, 2006, Vol. 203, p. 337-347).
For example, an oligopeptide compound Z-VRPR-fmk (Thome et al., Nature Immunology, 2008, Vol. 9, p. 272-281), phenylfuran derivatives (International Publication No. WO 2009/065897), phenothiazine derivatives (International Publication No. WO 2013/017637), triazole derivatives (Melnick et al., Cancer Cell, 2012, Vol. 22, p. 812-824), β-lapachone derivatives (Lim et al., Journal of Medicinal Chemistry, 2015, Vol. 58, p. 8491-8502) and pyrazolopyrimidine derivatives (International Publication No. WO 2015/181747) are known as compounds inhibiting the protease activity of MALT1.
On the other hand, for example, diphenylpyridine derivatives (JP Patent Publication (Kohyo) No. 2004-517870 A (2004)) as compounds having a cyclooxygenase inhibitory effect, selexipag; N-(2-(4-N-(5,6-diphenylpyrazin-2-yl)-N-isopropylamino)butoxy)acetyl)methanesulfonamide (International Publication No. WO 2002/088084) as a compound having prostaglandin 12 receptor agonism, N-((5,6-diphenylpyridin-3-yl)methylamine derivatives (International Publication No. WO 2006/042955) as compounds having a cannabinoid 1 receptor antagonistic effect, and pyrazine carbonyl guanidine derivatives (U.S. Pat. No. 3,313,813) as compounds having a diuretic effect have been reported as compounds having a diphenylpyridine, diphenylpyrimidine, diphenylpyridazine or diphenylpyrazine skeleton.
However, International Publication No. WO 2009/065897, International Publication No. WO 2013/017637, International Publication No. WO 2015/181747, JP Patent Publication (Kohyo) No. 2004-517870 A (2004), International Publication No. WO 2002/088084, International Publication No. WO 2006/042955 and U.S. Pat. No. 3,313,813 and Beyaert et al., Nature Immunology, 2008, Vol. 9, p. 263-271, Beyaert et al., The EMBO Journal, 2011, Vol. 30, p. 1742-1752, Staudt et al., Nature, 2006, Vol. 441, p. 106-110, Mak et al., The Journal of Clinical Investigation, 2012, Vol. 122, p. 4698-4709, Ma et al., Science, 2000, Vol. 289, p. 2350-2354, Klemm et al., The Journal of Experimental Medicine, 2006, Vol. 203, p. 337-347, Thome et al., Nature Immunology, 2008, Vol. 9, p. 272-281, Melnick et al., Cancer Cell, 2012, Vol. 22, p. 812-824 and Lim et al., Journal of Medicinal Chemistry, 2015, Vol. 58, p. 8491-8502 neither disclose that nor suggest the possibility that a guanidine derivative having a diphenylheteroaryl skeleton inhibits the protease activity of MALT1.
Accordingly, it could be helpful to provide a compound that inhibits the protease activity of MALT1 and exerts a therapeutic or prophylactic effect on autoimmune disease such as psoriasis or allergic disease such as atopic dermatitis.